Visualizing the protons in a metalloenzyme electron proton transfer pathway
| Autor: | Tobias E. Schrader, Reynier Suardíaz, Marc W. van der Kamp, Matthew P. Blakeley, Andreas Ostermann, Jaswir Basran, Hanna Kwon, Adrian J. Mulholland, Juliette M. Devos, Emma Lloyd Raven, Peter C. E. Moody |
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| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Models Molecular Proton proton transfer Protonation Electrons peroxidase Ascorbic Acid Heme 010402 general chemistry Photochemistry 01 natural sciences Redox Catalysis 03 medical and health sciences Electron transfer chemistry.chemical_compound Ascorbate Peroxidases neutron Oxidoreductase Metalloproteins heme abscorbate chemistry.chemical_classification Multidisciplinary Hydrogen bond Hydrogen Bonding Biological Sciences 0104 chemical sciences Neutron Diffraction 030104 developmental biology chemistry ddc:500 Protons Oxidation-Reduction |
| Zdroj: | Kwon, H, Basran, J, Devos, J M, Suardiaz Del Rio, R, Van Der Kamp, M W, Mulholland, A J, Schrader, T E, Ostermann, A, Blakeley, M P, Moody, P C E & Raven, E 2020, ' Visualizing the protons in a metalloenzyme electron proton transfer pathway ', Proceedings of the National Academy of Sciences of the United States of America . https://doi.org/10.1073/pnas.1918936117 Proceedings of the National Academy of Sciences of the United States of America 117(12), 6484-6490 (2020). doi:10.1073/pnas.1918936117 Proc Natl Acad Sci U S A |
| Popis: | In redox metalloenzymes, the process of electron transfer often involves the concerted movement of a proton. These processes are referred to as proton-coupled electron transfer, and they underpin a wide variety of biological processes, including respiration, energy conversion, photosynthesis, and metalloenzyme catalysis. The mechanisms of proton delivery are incompletely understood, in part due to an absence of information on exact proton locations and hydrogen bonding structures in a bona fide metalloenzyme proton pathway. Here, we present a 2.1-Å neutron crystal structure of the complex formed between a redox metalloenzyme (ascorbate peroxidase) and its reducing substrate (ascorbate). In the neutron structure of the complex, the protonation states of the electron/proton donor (ascorbate) and all of the residues involved in the electron/proton transfer pathway are directly observed. This information sheds light on possible proton movements during heme-catalyzed oxygen activation, as well as on ascorbate oxidation. |
| Databáze: | OpenAIRE |
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